anti-Poly(rC) Binding Protein 2 (PCBP2) Antikörper

Human Poly(rC) Binding Protein 2 (PCBP2) Interaktionspartner

1. PCBP2 appears to be an oncogenic splicing factor. A growing body of evidence has shown that PCBP1 regulates alternative splicing, translation, and RNA stability of many cancer-related genes. Taking together, PCBP1 has distinctive tumor suppressive functions, and increasing PCBP1 expression may represent a new approach for cancer treatment.

2. Results show that PCBP2 interacts with NLRX1 to participate in the NLRX1-induced degradation of MAVS and the inhibition of antiviral responses during HCV infection.

3. PCBP2 expression was markedly increased in higher stages of glioblastoma compared with those in lower stages; further research suggested that PCBP2 upregulation was connected with poorer prognosis in patients with glioblastoma

4. Double immunofluorescence for hnRNP E2 and TDP-43 showed most TDP-43 immunopositive dystrophic neuritis within frontal and temporal cortex, and the neuronal cytoplasmic inclusions seen in dentate gyrus granule cells, to contain hnRNP E2. Present findings indicate an association between TDP-43 and hnRNP E2 which might underlie the pathogenetic mechanism of Semantic Dementia Frontotemporal Lobar Degeneration.

5. Data suggest that the interaction between PCBP2 and the 3'UTR of the ARHGDIA mRNA may induce a local change in RNA structure that favors subsequent binding of miR-151-5p and miR-16, thus leading to the suppression of ARHGDIA expression.

6. To promote intracellular iron flux, an iron chaperone appears to be essential for receiving iron from heme catabolism. Data suggest that PCBP2 competes with CPR for binding HO1; PCBP2 K homology 3 domain is important for HO1/PCBP2 interaction; heme prompts HO1/CPR multimer and decreases HO1/PCBP2 multimer. [PCBP2 = poly(rC) binding protein 2; CPR = cytochrome P450 reductase; HO1 = heme oxidase 1]

7. BC200 RNA interacts with hnRNP E1 and E2 mainly through its unique 3' C-rich domain.

8. Study determined that PCBP2 specifically associates with components of this kinase cascade and regulates the activities of its downstream transcriptional coactivators.

9. These results suggest that FPN1 exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process.

10. PCBP2 was overexpressed in esophageal squamous cell carcinoma tissues and cell lines. PCBP2 expression promoted proliferation of ESCC cells. We also found that reduced PCBP2 expression might induce ESCC cell apoptosis with increased cleaved caspase3 expression. Overall, our findings indicated that PCBP2 might be involved in the ESCC progression and be considered as a new treatment target in ESCC.

11. High expression of PCBP2 may contribute to sorafenib resistance in hepatocellular carcinoma cells.

12. our data indicate that miR-214 may function as tumor suppressor in glioma by targeting PCBP2

13. alphaCP1/ alphaCP2 binding to a cytosine-rich subset of polypyrimidine tracts drives a novel pathway of cassette exon splicing in the mammalian transcriptome.

14. beta2-adrenergic receptor signaling promotes pancreatic ductal adenocarcinoma progression by facilitating PCBP2-dependent c-myc expression.

15. PCBP2 knockdown promoted angiotensin II-induced hypertrophy (increase in cell size, protein synthesis and activation of fetal genes) of cardiomyocytes, while PCBP2 overexpression obtained oppose effects.

16. Protein and mRNA levels of PCBP2 were down-regulated under insulin-resistant conditions. Over-expression of PCBP2 inhibits HIF1alpha and STAT3 pathway.

17. STAT3 functions via cellular PCBP2 to regulate B-cell lytic susceptibility by restraining Epstein-Barr Virus lytic activation.

18. PCBP1 and PCBP2 may serve as iron chaperones to multiple classes of cytosolic nonheme iron enzymes and may have a particular role in restoring metal cofactors that are spontaneously lost in iron deficient cells.

19. PCBP2-depletion induces apoptosis in gastric cancer cells via up-regulating expression of pro-apoptotic proteins and down-regulating anti-apoptotic proteins. miR-34a is a target of PCBP2, and miR-34a is critically essential for the function of PCBP2.

20. SIRT6 inhibits glioma cell proliferation and colony formation in vitro and glioma cell growth in vivo in a PCBP2 dependent manner. SIRT6 inhibits PCBP2 expression through deacetylating H3K9ac and SIRT6 acts as a tumor suppressor in glioma.

Mouse (Murine) Poly(rC) Binding Protein 2 (PCBP2) Interaktionspartner

1. Embryos lacking the KH domain poly(C) binding protein, Pcbp2, are selectively deficient in the definitive erythroid lineage. Compared to wild-type controls, transcript splicing analysis of the Pcbp2(-/-) embryonic liver reveals accentuated exclusion of an exon (exon 6) that encodes a highly conserved transcriptional control segment of the hematopoietic master regulator, Runx1.

2. These findings suggest that Hr mRNA expression is regulated at the post-transcriptional level via IRES-mediated translation control through interaction with PCPB2, but not in MUHH.

3. Study determined that PCBP2 specifically associates with components of this kinase cascade and regulates the activities of its downstream transcriptional coactivators.

4. data suggest that PCBP2 regulates p73 expression via mRNA stability and p73-dependent biological function in ROS production and cellular senescence.

5. PCBP2 overexpression rescues the Meis1 effects of Akt-mTOR pathway and hypertrophy of cardiomyocytes.

6. These data reveal that Pcbp1 and Pcbp2 are individually essential for mouse embryonic development and have distinct impacts on embryonic viability and that Pcpb2 has a nonredundant in vivo role in hematopoiesis.

7. PCBP2 knockdown promoted angiotensin II-induced hypertrophy (increase in cell size, protein synthesis and activation of fetal genes) of cardiomyocytes, while PCBP2 overexpression obtained oppose effects.

8. Our analysis of PCBP1 and PCBP2 expression demonstrates robust expression of these two proteins within the gastric epithelium with high concordance for both proteins in their cell-type specificities and intracellular distributions.

9. This study demonstrates for the first time that alpha-CP2 functions as a transcriptional activator by binding to a single-stranded poly(C) sequence.

10. This study provides evidence that PCBP2 and hnRNP A1 bind to the 5' and 3' ends of the murine norovirus 1 viral RNA and contribute to RNA circularization, playing a role in the virus life cycle.

11. PCBP2-AIP4 axis defines a new signaling cascade for MAVS degradation and 'fine tuning' of antiviral innate immunity.

Pig (Porcine) Poly(rC) Binding Protein 2 (PCBP2) Interaktionspartner

1. These results indicated that Nsp1beta of porcine reproductive and respiratory syndrome virus is able to bind and interact with cellular PCBP2 strongly in both the infected cells and plasmid transfected cells.

2. Overall, the results presented here point toward an important role for PCBP1 and PCBP2 in regulating porcine reproductive and respiratory syndrome virus RNA synthesis via binding to viral nonstructural protein 1beta.